SAXSdb — 1elu

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1. Protein Identity and Related Structures Protein Identity & Related Structures

L-CYSTEINE/L-CYSTINE C-S LYASE

Synechocystis sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	POTASSIUM ION × 2 2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC ACID × 2 S-MERCAPTOCYSTEINE × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9ZHG9_SYNY4
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 9–390； UniProt 12–393 Author chain B； PDBConstruct 9–390； UniProt 12–393

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1elu
Deposition date deposition_date	2000-03-14
Structure title title	COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.
Keywords keywords	;FeS cluster biosynthesis, pyridoxal 5'-phosphate, thiocysteine, aminoacrylate, enzyme-product complex, LYASE ;; LYASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1elu__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1elu__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1elu__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	28.04 Å
Rg (electron density)	27.02 Å
Total Rg	27.81 Å
Atom count	5928
Residues	762
Excluded volume	105220 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1elu__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	L-CYSTEINE/L-CYSTINE C-S LYASE
Molecular weight formula_weight	42846.6 kDa
Mutation mutation	MADPVNLIPDR TO MTMITPSL
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6680

MTMITPSLHQFPGLANKTYFNFGGQGILPTVALEAITAMYGYLQENGPFSIAANQHIQQLIAQLRQALAETFNVDPNTITITDNVTTGCDIVLWGLDWHQGDEILLTDCEHPGIIAIVQAIAARFGITYRFFPVAATLNQGDAAAVLANHLGPKTRLVILSHLLWNTGQVLPLAEIMAVCRRHQGNYPVRVLVDGAQSAGSLPLDFSRLEVDYYAFTGHKWFAGPAGVGGLYIHGDCLGEINPTYVGWRSITYGAKGEPTGWAEGGKRFEVATSAYPQYAGLLAALQLHQRQGTAEERYQAICQRSEFLWRGLNQLPHVHCLATSAPQAGLVSFTVDSPLGHRAIVQKLEEQRIYLRTIADPDCIRACCHYITDEEEINHLLARLADFGP

Source Source

Source organism organism	Synechocystis sp.
NCBI taxonomy ID ncbi_taxonomy_id	1147
Host organism host_organism	Bacteria

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC ACID
Molecular weight formula_weight	320.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	S-MERCAPTOCYSTEINE
Molecular weight formula_weight	153.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	752

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1elua_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.3 — Cystathionine synthase-like

Domain ID domain_id	d1elub_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.3 — Cystathionine synthase-like

CATH v4.4 (4 domains)

Domain ID domain_id	1eluA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	10 — Aspartate Aminotransferase, domain 1

Domain ID domain_id	1eluA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily	10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Domain ID domain_id	1eluB01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	10 — Aspartate Aminotransferase, domain 1

Domain ID domain_id	1eluB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily	10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)

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Unit-cell length a length_a	62.448 Å
Unit-cell length b length_b	65.386 Å
Unit-cell length c length_c	170.532 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.550 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2180
R_work r_work	0.2140
R_free r_free	0.2590

COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.

1. Protein Identity and Related Structures Protein Identity & Related Structures

L-CYSTEINE/L-CYSTINE C-S LYASE

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1elu__assembly_1__model_1

1elu__assembly_1__model_1 | I(q)

1elu__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)

COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.

1. Protein Identity and Related Structures Protein Identity & Related Structures

L-CYSTEINE/L-CYSTINE C-S LYASE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1elu__assembly_1__model_1

1elu__assembly_1__model_1 | I(q)

1elu__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)